Intracellular antibody signalling is regulated by phosphorylation of the Fc receptor TRIM21

Autor: Claire Dickson, Adam J Fletcher, Marina Vaysburd, Ji-Chun Yang, Donna L Mallery, Jingwei Zeng, Christopher M Johnson, Stephen H McLaughlin, Mark Skehel, Sarah Maslen, James Cruickshank, Nicolas Huguenin-Dezot, Jason W Chin, David Neuhaus, Leo C James

Publikováno v: eLife, Vol 7 (2018)

Cell surface Fc receptors activate inflammation and are tightly controlled to prevent autoimmunity. Antibodies also simulate potent immune signalling from inside the cell via the cytosolic antibody receptor TRIM21, but how this is regulated is unknow

Externí odkaz: https://doaj.org/article/5202b947b0ec499ebb78db70bf28d54e

Structure of the SAS-6 cartwheel hub from Leishmania major

Autor: Mark van Breugel, Rainer Wilcken, Stephen H McLaughlin, Trevor J Rutherford, Christopher M Johnson

Publikováno v: eLife, Vol 3 (2014)

Centrioles are cylindrical cell organelles with a ninefold symmetric peripheral microtubule array that is essential to template cilia and flagella. They are built around a central cartwheel assembly that is organized through homo-oligomerization of t

Externí odkaz: https://doaj.org/article/cef7a151909f416f85fda12a6d616c05

A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases

Autor: Leo Kiss, Jingwei Zeng, Claire F. Dickson, Donna L. Mallery, Ji-Chun Yang, Stephen H. McLaughlin, Andreas Boland, David Neuhaus, Leo C. James

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)

The E3 ligase TRIM21 targets a broad range of pathogenic proteins using a unique mechanism. Here, the authors combine structural, biochemical and cell biological approaches to elucidate how TRIM21 selectively recruits its canonical E2 partner enzyme

Externí odkaz: https://doaj.org/article/470293ee22be4d32ba89b9430667e524

Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly

Autor: Yi Liu, Gagan D. Gupta, Deepak D. Barnabas, Fikret G. Agircan, Shahid Mehmood, Di Wu, Etienne Coyaud, Christopher M. Johnson, Stephen H. McLaughlin, Antonina Andreeva, Stefan M. V. Freund, Carol V. Robinson, Sally W. T. Cheung, Brian Raught, Laurence Pelletier, Mark van Breugel

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)

Centriole duplication is tightly regulated in vivo, but the underlying molecular mechanisms are incompletely understood. Here the authors use high-resolution structural and imaging methods to show that CEP85 directly interacts with STIL and mediates

Externí odkaz: https://doaj.org/article/64d5bf6e3d9f4b17ae080b2ad6edfff9

The DNA-damage kinase ATR activates the FANCD2-FANCI clamp by priming it for ubiquitination

Autor: Tamara Sijacki, Pablo Alcón, Zhuo A. Chen, Stephen H. McLaughlin, Shabih Shakeel, Juri Rappsilber, Lori A. Passmore

Publikováno v: Nat Struct Mol Biol
Sijacki, T, Alcón, P, Chen, Z A, Mclaughlin, S H, Shakeel, S, Rappsilber, J & Passmore, L A 2022, ' The DNA-damage kinase ATR activates the FANCD2-FANCI clamp by priming it for ubiquitination ', Nature Structural & Molecular Biology, vol. 29, no. 9, pp. 881-890 . https://doi.org/10.1038/s41594-022-00820-9

DNA interstrand crosslinks are tumor-inducing lesions that block DNA replication and transcription. When crosslinks are detected at stalled replication forks, ATR kinase phosphorylates FANCI, which stimulates monoubiquitination of the FANCD2-FANCI cl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29732b28545880318807cd1c9a4253b6
https://doi.org/10.1038/s41594-022-00820-9